Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.3.1.21 - carnitine O-palmitoyltransferase and Organism(s) Homo sapiens

for references in articles please use BRENDA:EC2.3.1.21
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Broad specificity to acyl group, over the range C8 to C18; optimal activity with palmitoyl-CoA. cf. EC 2.3.1.7 carnitine O-acetyltransferase and EC 2.3.1.137 carnitine O-octanoyltransferase.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
cpt1a, carnitine palmitoyltransferase, cpt i, carnitine palmitoyltransferase i, cpt-1, cpt ii, cpt1b, carnitine palmitoyltransferase 1, carnitine palmitoyltransferase-1, cpt1c, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acylcarnitine transferase
-
-
-
-
carnitine palmitoyl transferase 1A
-
-
carnitine palmitoyl transferase-1A
-
carnitine palmitoyltransferase
-
-
-
-
carnitine palmitoyltransferase 1
-
-
carnitine palmitoyltransferase 1A
-
-
carnitine palmitoyltransferase 1B
-
-
carnitine palmitoyltransferase 2
carnitine palmitoyltransferase I
carnitine palmitoyltransferase IA
-
-
carnitine palmitoyltransferase II
carnitine palmitoyltransferase-1
carnitine palmitoyltransferase-A
-
-
-
-
carnitine palmitoyltransferases 2
ubiquitous protein
CPT
-
-
-
-
CPT-1
-
-
CPT-A
-
-
-
-
CPT-B
-
-
-
-
CPT1-A
liver isoenzyme
CPT1-B
-
muscle isoenzyme
CPT1-C
-
brain isoenzyme
CPT1A
L-carnitine palmitoyltransferase
-
-
-
-
M-CPTI
muscle carnitine palmitoyltransferase I
-
-
palmitoylcarnitine transferase
-
-
-
-
palmitoyltransferase, carnitine
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
show the reaction diagram
the catalytic triad is composed of Cys305, His473, and Asp454, with Cys305 serving as a probable nucleophile, thus acting as a site for covalent attachment of the acyl molecule and formation of a stable acyl-enzyme intermediate, mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
palmitoyl-CoA:L-carnitine O-palmitoyltransferase
Broad specificity to acyl group, over the range C8 to C18; optimal activity with palmitoyl-CoA. cf. EC 2.3.1.7 carnitine O-acetyltransferase and EC 2.3.1.137 carnitine O-octanoyltransferase.
CAS REGISTRY NUMBER
COMMENTARY hide
9068-41-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4,8-dimethylnonanoyl-CoA + L-carnitine
?
show the reaction diagram
-
-
-
?
4,8-dimethylnonanoyl-CoA + L-carnitine
CoA + 4,8-dimethylnonanoyl-L-carnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
arachidoyl-CoA + L-carnitine
CoA + L-arachidoylcarnitine
show the reaction diagram
-
-
-
-
?
decanoyl-CoA + L-carnitine
CoA + L-decanoylcarnitine
show the reaction diagram
dodecanoyl-CoA + L-carnitine
CoA + L-dodecanoylcarnitine
show the reaction diagram
-
-
-
?
erucoyl-CoA + L-carnitine
CoA + L-erucoylcarnitine
show the reaction diagram
-
-
-
-
?
hexanoyl-CoA + L-carnitine
CoA + L-hexanoylcarnitine
show the reaction diagram
-
-
-
r
L-carnitine + palmitoyl-CoA
L-palmitoylcarnitine + CoA
show the reaction diagram
lauroyl-CoA + L-carnitine
CoA + L-lauroylcarnitine
show the reaction diagram
linoleoyl-CoA + L-carnitine
CoA + L-linoleoylcarnitine
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + L-carnitine
CoA + L-myristoylcarnitine
show the reaction diagram
octanoyl-CoA + L-carnitine
CoA + L-octanoylcarnitine
show the reaction diagram
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
stearoyl-CoA + L-carnitine
CoA + L-stearoylcarnitine
show the reaction diagram
trans-2-hexadecenoyl-CoA + L-carnitine
CoA + trans-2-hexadecenoyl-L-carnitine
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-bromopalmitoyl-CoA
-
with addition of carnitine
acetyl-CoA
-
-
arachidonic acid
-
the enzymatic activity significantly declines by treatment with 0.1 mM for 1 h
C75-CoA
-
potent competitive inhibition, IC50: 0.00025 mM in INS(832/13) cells, IC50: 0.00046 in L6E9 myotubes, binds tightly but reversibly to CPT I, C75 applied in vivo is transformed to C75-CoA and inhibits fatty acid oxidation, e.g. in pancreatic INS(823/13), muscle L6E9, or kidney HEK293 cell lines, inhibition mechanism, overview, molecular model of docking of C75-CoA to L-CPT I
CoA esters of certain oxirane carboxylic acids
-
irreversible, CPT I but not CPT II
-
etomoxir
etomoxiryl-CoA
-
IC50: 0.00121 mM in INS(832/13) cells, IC50: 0.00287 in L6E9 myotubes
H2O2
-
the enzymatic activity significantly and reversibly declines by 1 mM H2O2
L-aminocarnitine
-
inhibition of CPT II not CPT I
malonyl CoA
-
a physiological CPT1 inhibitor
malonyl-CoA
octyl glucoside
-
complete loss of CPT I activity, no loss of CPT II activity
oxfenicine
-
-
palmitoyl-CoA
thermally destabilizes bith wild-type and mutant S113L
rotenone
-
the enzymatic activity significantly declines by treatment with 0.001 mM for 2 h
trans-2-hexadecenoyl-CoA
competitive
Triton X-100
tumor necrosis factor-alpha
-
the enzymatic activity significantly declines by treatment with 25 ng/ml for 30 min
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
C-75
-
i.e. 3-carboxy-4-alkyl-2-methylenebutyrolactone, physiologic enzyme stimulation, regulatory effects, overview
C75
-
a potential drug for the treatment of obesity, a competitive, irreversible inhibitor of fatty acid synthase, and a malonyl-CoA analogue that antagonizes the allosteric inhibitory effect of malonyl-CoA on CPT I
daidzein
-
activates 5.5fold, induces the enzyme expression
genistein
-
activates 3fold alone, and about 6fold in concert with L-carnitine, induces the enzyme expression
L-carnitine
-
activates 3fold alone, and about 6fold in concert with genistein, induces the enzyme expression
additional information
-
clofibrate induces the enzyme expression in transfected Huh-7 cells
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017
decanoyl-CoA
-
-
0.152
hexanoyl-CoA
-
-
0.056 - 1.588
L-carnitine
1.139
L-octanoylcarnitine
-
-
0.123
L-palmitoylcarnitine
-
-
0.011
lauroyl-CoA
-
-
0.031
myristoyl-CoA
-
-
0.023
octanoyl-CoA
-
-
0.0062 - 0.4
palmitoyl-CoA
0.018
stearoyl-CoA
-
-
0.0081
trans-2-hexadecenoyl-CoA
pH 7.4, 37°C
additional information
additional information
-
Km values for carnitine with different acyl-CoA substrates
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.045
acetyl-CoA
-
-
0.045
CoA
-
-
0.0035
L-aminocarnitine
-
CPT II
0.00022
malonyl-CoA
-
-
0.0188
trans-2-hexadecenoyl-CoA
pH 7.4, 37°C
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00025 - 0.00046
C75-CoA
0.00121 - 0.00287
etomoxiryl-CoA
Homo sapiens
-
IC50: 0.00121 mM in INS(832/13) cells, IC50: 0.00287 in L6E9 myotubes
0.00003 - 0.0384
malonyl-CoA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00018
mutant enzyme F352C/V368I, at 30°C, pH not specified in the publication
0.00027
mutant enzyme V368I, at 30°C, pH not specified in the publication
0.00028
wild type enzyme, at 30°C, pH not specified in the publication
0.00062
F352C/V368I/V605L mutant protein, COS-7 cell lysate
0.00063
wild-type protein and F352C/V368I/V605L mutant protein, COS-7 cell lysate (doubly transfected)
0.00071
P504L/V605L mutant protein, COS-7 cell lysate
0.00072
0.00073
F352C mutant protein, COS-7 cell lysate
0.00076
P504L mutant protein, COS-7 cell lysate
0.00078
V605L mutant protein, COS-7 cell lysate
0.00081
M647V mutant protein, COS-7 cell lysate
0.00085
V368I mutant protein, COS-7 cell lysate
0.00087
wild-type protein, COS-7 cell lysate
0.00227
-
mitochondrial fraction, wild-type protein expressed in COS-7 cell
0.0028
-
recombinant revertant A305C
0.0029
-
recombinant wild-type enzyme
0.00443
-
wild-type protein, mitochondrial preparation
0.00943
-
chimeric protein: residues 1-50 of pig enzyme recombined with human enzyme, mitochondrial preparation
0.01059
-
chimeric protein: residues 1-128 of pig enzyme recombined with human enzyme, mitochondrial preparation
33
mutant S113L, pH 7.4, 30°C
39
wild-type, pH 7.4, 30°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1
-
assay at
7.4
-
assay at
7.5
-
assay at
7.6
-
assay at
8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
low level of expression of CPT1-C
Manually annotated by BRENDA team
-
kidney cell line
Manually annotated by BRENDA team
-
pancreatic cell line
Manually annotated by BRENDA team
low level of expression of CPT1-C
Manually annotated by BRENDA team
low level of expression of CPT1-C
Manually annotated by BRENDA team
-
CPT II, M-CPT I
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
forward reaction by CPT I at outer mitochondrial membrane, transport of acylcarnitine through mitochondrial membrane, reverse reaction at inner face of inner membrane by CPT II, overview
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CPT1A_HUMAN
773
2
88368
Swiss-Prot
other Location (Reliability: 4)
CPT1B_HUMAN
772
2
87801
Swiss-Prot
other Location (Reliability: 3)
CPT1C_HUMAN
803
2
90989
Swiss-Prot
other Location (Reliability: 3)
CPT2_HUMAN
658
0
73777
Swiss-Prot
Mitochondrion (Reliability: 1)
A0A024QZI3_HUMAN
792
2
89713
TrEMBL
other Location (Reliability: 3)
A5PLL0_HUMAN
772
2
87702
TrEMBL
other Location (Reliability: 3)
A0A024R5F4_HUMAN
773
2
88368
TrEMBL
other Location (Reliability: 4)
Q53FV7_HUMAN
772
2
87786
TrEMBL
other Location (Reliability: 3)
B2RAQ8_HUMAN
773
2
88340
TrEMBL
other Location (Reliability: 4)
A8K5K1_HUMAN
772
2
87827
TrEMBL
other Location (Reliability: 3)
A0A024QZE3_HUMAN
803
2
90989
TrEMBL
other Location (Reliability: 3)
A0A024R4W7_HUMAN
772
2
87801
TrEMBL
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
274000
-
gel filtration
66000
-
4 * 66000, SDS-PAGE
88200
-
x * 88200, isozymes L-CPT1 and M-CPT1
additional information
-
amino acid sequence of peptides
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 88200, isozymes L-CPT1 and M-CPT1
homotetramer
-
tetramer
-
4 * 66000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A305C
-
site-directed mutagenesis, the revertant mutant shows about wild-type activity
A478G
-
site-directed mutagenesis, the mutant shows decreased sensitivity to malonyl-CoA compared to the wild-type enzyme
C304A
-
reduced expression in COS-7 cell, reduced activity
C304W
-
reduced expression in COS-7 cell, reduced activity
C305A
C305D
-
73% of wild-type activity in mitochondrial fraction (COS-7 cell), 81% of wild-type expression in COS-7 cell
C305E
-
50% of wild-type expression in COS-7 cell
C305F
-
about 20% of wild-type expression in COS-7 cell
C305G
-
about 5% of wild-type expression in COS-7 cell
C305H
-
38% of wild-type activity in mitochondrial fraction in COS-7 cell
C305I
-
4% of wild-type activity in mitochondrial fraction in COS-7 cell
C305K
-
about 25% of wild-type expression in COS-7 cell
C305L
-
about 20% of wild-type expression in COS-7 cell
C305M
-
about 20% of wild-type expression in COS-7 cell
C305N
-
about 10% of wild-type expression in COS-7 cell
C305P
-
about 20% of wild-type expression in COS-7 cell
C305Q
-
about 30% of wild-type expression in COS-7 cell
C305R
-
about 20% of wild-type expression in COS-7 cell
C305S
-
about 20% of wild-type expression in COS-7 cell
C305T
-
about 10% of wild-type expression in COS-7 cell
C305V
-
about 25% of wild-type expression in COS-7 cell
C305W
-
8% of wild-type activity in mitochondrial fraction, 30% of wild-type expression in COS-7 cell
C305Y
-
about 20% of wild-type expression in COS-7 cell
C448A
-
site-directed mutagenesis, the mutant shows unaltered catalytic activity and sensitivity to malonyl-CoA compared to the wild-type enzyme
C504A
-
site-directed mutagenesis, the mutant shows unaltered catalytic activity and sensitivity to malonyl-CoA compared to the wild-type enzyme
C526A
-
site-directed mutagenesis, the mutant shows unaltered catalytic activity but increased sensitivity to malonyl-CoA compared to the wild-type enzyme
C548S
-
site-directed mutagenesis, the mutant shows unaltered catalytic activity and sensitivity to malonyl-CoA compared to the wild-type enzyme
C562A
-
site-directed mutagenesis, the mutant shows unaltered catalytic activity and sensitivity to malonyl-CoA compared to the wild-type enzyme
C586A
-
site-directed mutagenesis, the mutant shows unaltered catalytic activity but reduced sensitivity to malonyl-CoA compared to the wild-type enzyme
C608A
-
site-directed mutagenesis, the mutant shows unaltered catalytic activity and sensitivity to malonyl-CoA compared to the wild-type enzyme
C659A
-
site-directed mutagenesis, the mutant shows unaltered catalytic activity but increased sensitivity to malonyl-CoA compared to the wild-type enzyme
D17E
-
pig protein: Glu in this position
DELTA1-18/V19A/L23A/S24A
-
143fold increase in IC50 for malonyl-CoA, 1.4fold decrease in KM-value for carnitine, 4fold increase in Km-value for palmitoyl-CoA
DELTA563-772
mitochondria from Pichia pastoris expressing the deletion mutant have no CPTI activity
DELTA659-772
mitochondria from Pichia pastoris expressing the deletion mutant have no CPTI activity
DELTA728-772
mitochondria from Pichia pastoris expressing the deletion mutant have no CPTI activity
DELTA752-772
mitochondria from Pichia pastoris expressing the deletion mutant have no CPTI activity
DELTA762-772
mitochondria from Pichia pastoris expressing the deletion mutant have no CPTI activity
DELTA763-772
mitochondria from Pichia pastoris expressing the deletion mutant have no CPTI activity
DELTA766-772
activity of the mutant is similar to wild-type enzyme
DELTA769-772
activity of the mutant is similar to wild-type enzyme
E26K
-
site-directed mutagenesis, the mutant shows decreased sensitivity to malonyl-CoA compared to the wild-type enzyme
E26K/K561E
-
site-directed mutagenesis, the double mutant shows the same sensitivity to malonyl-CoA compared to the wild-type enzyme
E3A/H5A/V19A/L23A/S24A
-
97fold increase in IC50 for malonyl-CoA, 1.4fold decrease in KM-value for carnitine, 11fold decrease in Km-value for palmitoyl-CoA
E3A/V19A/L23A/S24A
-
143fold increase in IC50 for malonyl-CoA, 1.3fold decrease in KM-value for carnitine, 8.7fold decrease in Km-value for palmitoyl-CoA
E531K
-
naturally occuring mutation
F352C
F352C/V368I
F352C/V368I/V605L
triple mutant with naturally occuring mutations
H5A
-
2.1fold increase in IC50 for malonyl-CoA, 1.1fold increase in KM-value for carnitine, 1.7fold decrease in Km-value for palmitoyl-CoA
I66V
-
naturally occuring mutation
I66V/E531K
-
naturally occuring mutation, activity is not markedly different from wild-type enzyme, sensitivity toward malonyl-CoA is not markedly different from the sensitivity of wild-type enzyme
I66V/S427C
-
naturally occuring mutation, activity is not markedly different from wild-type enzyme, sensitivity toward malonyl-CoA is not markedly different from the sensitivity of wild-type enzyme
K561E
-
site-directed mutagenesis, the mutant shows decreased sensitivity to malonyl-CoA compared to the wild-type enzyme
L264A
60.4% of the wild-type activity
L764R
L764V
as active as the wild-type enzyme
M593S
-
site-directed mutagenesis, the mutant is insensitive to malonyl-CoA
M647V
naturally occuring mutation
P479L
-
naturally occuring mutation, reduced enzyme activity
P504L
naturally occuring mutation
P504L/V605L
double mutant with naturally occuring mutations
R243T
-
site-directed mutagenesis, the mutant shows highly decreased sensitivity to malonyl-CoA compared to the wild-type enzyme
R243T/A478G
-
site-directed mutagenesis, the mutant shows highly decreased sensitivity to malonyl-CoA compared to the wild-type enzyme
S113L
S427C
-
naturally occuring mutation, activity is not markedly different from wild-type enzyme, sensitivity toward malonyl-CoA is not markedly different from the sensitivity of wild-type enzyme
V368I
V605L
naturally occuring mutation
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Triton X-100: erythrocyte plasma membrane enzyme is stable, enzyme from microsomes and mitochondrial outer membrane not
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme partially by microsome preparation
-
recombinant M-CPT I from Pichia pastoris
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in COS-7 cell
expressed in Pichia pastoris
-
expressed in the distal hindlimb muscles of Rattus norvegicus
expression in rat brown adipocyte cell line
expression in Saccharomyces cerevisiae
expression of wild-type and mutant isozyme CPT1A in Saccharomyces cerevisiae
-
expression of wild-type and mutant isozymes M-CPT I in Pichia pastoris strain GS115
-
gene CPT 1B, overexpression in isolated extensor digitorum longus, EDL, muscle strips, electrotransfection
-
isozymes CPT1 and CPT2
-
mutant enzymes expressed in Pichia pastoris
overexpression of M-CPT I in Pichia pastoris, containing about 24 copies of the expression vector
-
quantitative expression analysis, expression in Huh-7 cells, treatment with clofibrate induces the enzyme expression
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform CPT1C expression is frequently up-regulated in human lung tumors. CPT1C can be induced by hypoxia or glucose deprivation and is regulated by AMPKalpha
mitochondrial CPT1 proteins are targeted for inactivation by diverse oxidants or oxidative stress in human cells
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of detergent-inactivated recombinant M-CPT I, purified from Pichia pastoris, by removal of detergents in presence of phospholipids
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zierz, S.; Engel, A.G.
Different sites of inhibition of carnitine palmitoyltransferase by malonyl-CoA, and by acetyl-CoA and CoA, in human skeletal muscle
Biochem. J.
245
205-209
1987
Homo sapiens
Manually annotated by BRENDA team
Ramsay, R.R.; Mancinelli, G.; Arduini, A.
Carnitine palmitoyltransferase in human erythrocyte membrane. Properties and malonyl-CoA sensitivity
Biochem. J.
275
685-688
1991
Homo sapiens
Manually annotated by BRENDA team
Finocchiaro, G.; Colombo, I.; DiDonato, S.
Purification, characterization and partial amino acid sequences of carnitine palmitoyl-transferase from human liver
FEBS Lett.
274
163-166
1990
Homo sapiens
Manually annotated by BRENDA team
Woeltje, K.F.; Esser, V.; Weis, B.C.; Cox, W.F.; Schroeder, J.G.; Liao, S.L.; Foster, D.W.; McGarry, J.D.
Inter-tissue and inter-species characteristics of the mitochondrial carnitine palmitoyltransferase enzyme system
J. Biol. Chem.
265
10714-10719
1990
Homo sapiens, Platyrrhini, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Zhu, H.; Shi, J.; Cregg, J.M.; Woldegiorgis, G.
Reconstitution of highly expressed human heart muscle carnitine palmitoyltransferase I
Biochem. Biophys. Res. Commun.
239
498-502
1997
Homo sapiens
Manually annotated by BRENDA team
Brown, N.F.; Hill, J.K.; Esser, V.; Kirkland, J.L.; Corkey, B.E.; Foster, D.W.; McGarry, J.D.
Mouse white adipocytes and 3T3-L1 cells display an anomalous pattern of carnitine palmitoyltransferase (CPT) I isoform expression during differentiation. Inter-tissue and inter-species expression of CPT I and CPT II enzymes
Biochem. J.
327
225-231
1997
Homo sapiens, Mesocricetus auratus, Mus musculus, Rattus norvegicus
-
Manually annotated by BRENDA team
Hertel, K.; Gellerich, F.N.; Hein, W.; Zierz, S.
Kinetic investigation of carnitine palmitoyltransferases in homogenates of human skeletal muscle using L-amino-carnitine and malonyl-CoA
Adv. Exp. Med. Biol.
466
87-93
1999
Homo sapiens
Manually annotated by BRENDA team
Eaton, S.; Fukumoto, K.; Paladio Duran, N.; Pierro, A.; Spitz, L.; Quant, P.A.; Bartlett, K.
Carnitine palmitoyl transferase I and the control of myocardial beta-oxidation flux
Biochem. Soc. Trans.
29
245-250
2001
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Haap, M.; Thamer, C.; Machann, J.; Tschritter, O.; Loblein, K.; Kellerer, M.; Schick, F.; Jacob, S.; Haring, H.U.; Stumvoll, M.
Metabolic characterization of a woman homozygous for the Ser113Leu missense mutation in carnitine palmitoyl transferase II
J. Clin. Endocrinol. Metab.
87
2139-2143
2002
Homo sapiens
Manually annotated by BRENDA team
Zhu, H.; Shi, J.; Treber, M.; Dai, J.; Arvidson, D.N.; Woldegiorgis, G.
Substitution of glutamate-3, valine-19, leucine-23, and serine-24 with alanine in the N-terminal region of human heart muscle carnitine palmitoyltransferase I abolishes malonyl CoA inhibition and binding
Arch. Biochem. Biophys.
413
67-74
2003
Homo sapiens
Manually annotated by BRENDA team
Dai, J.; Zhu, H.; Woldegiorgis, G.
Leucine-764 near the extreme C-terminal end of carnitine palmitoyltransferase I is important for activity
Biochem. Biophys. Res. Commun.
301
758-763
2003
Homo sapiens (Q92523)
Manually annotated by BRENDA team
Bonnefont, J.P.; Djouadi, F.; Prip-Buus, C.; Gobin, S.; Munnich, A.; Bastin, J.
Carnitine palmitoyltransferases 1 and 2: biochemical, molecular and medical aspects
Mol. Aspects Med.
25
495-520
2004
Homo sapiens, Homo sapiens (P23786), Homo sapiens (P50416)
Manually annotated by BRENDA team
Bruce, C.R.; Brolin, C.; Turner, N.; Cleasby, M.E.; van der Leij, F.R.; Cooney, G.J.; Kraegen, E.W.
Overexpression of carnitine palmitoyltransferase I in skeletal muscle in vivo increases fatty acid oxidation and reduces triacylglycerol esterification
Am. J. Physiol. Endocrinol. Metab.
292
E1231-E1237
2007
Homo sapiens
Manually annotated by BRENDA team
Bentebibel, A.; Sebastian, D.; Herrero, L.; Lopez-Vinas, E.; Serra, D.; Asins, G.; Gomez-Puertas, P.; Hegardt, F.G.
Novel effect of C75 on carnitine palmitoyltransferase I activity and palmitate oxidation
Biochemistry
45
4339-4350
2006
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Tamaoki, Y.; Kimura, M.; Hasegawa, Y.; Iga, M.; Inoue, M.; Yamaguchi, S.
A survey of Japanese patients with mitochondrial fatty acid beta-oxidation and related disorders as detected from 1985 to 2000
Brain Dev.
24
675-680
2002
Homo sapiens
Manually annotated by BRENDA team
Kuhajda, F.P.; Ronnett, G.V.
Modulation of carnitine palmitoyltransferase-1 for the treatment of obesity
Curr. Opin. Investig. Drugs
8
312-317
2007
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Shin, E.S.; Cho, S.Y.; Lee, E.H.; Lee, S.J.; Chang, I.S.; Lee, T.R.
Positive regulation of hepatic carnitine palmitoyl transferase 1A (CPT1A) activities by soy isoflavones and L-carnitine
Eur. J. Nutr.
45
159-164
2006
Homo sapiens, Mus musculus, Mus musculus C57/BL6J
Manually annotated by BRENDA team
Liu, H.; Zheng, G.; Treber, M.; Dai, J.; Woldegiorgis, G.
Cysteine-scanning mutagenesis of muscle carnitine palmitoyltransferase I reveals a single cysteine residue (Cys-305) is important for catalysis
J. Biol. Chem.
280
4524-4531
2005
Homo sapiens
Manually annotated by BRENDA team
Lopez-Vinas, E.; Bentebibel, A.; Gurunathan, C.; Morillas, M.; de Arriaga, D.; Serra, D.; Asins, G.; Hegardt, F.G.; Gomez-Puertas, P.
Definition by functional and structural analysis of two malonyl-CoA sites in carnitine palmitoyltransferase 1A
J. Biol. Chem.
282
18212-18224
2007
Homo sapiens
Manually annotated by BRENDA team
Ratheiser, K.; Schneeweiss, B.; Waldhaeusl, W.; Fasching, P.; Korn, A
Nowotny, P.; Rohac, M.; Wolf, H.P.O.: Inhibition by etomoxir of carnitine palmitoyltransferase I reduces hepatic glucose production and plasma lipids in non-insulin-dependent diabetes mellitus
Metabolism
40
1185-1190
1991
Homo sapiens
Manually annotated by BRENDA team
Yamazaki, N.; Matsuo, T.; Kurata, M.; Suzuki, M.; Fujiwaki, T.; Yamaguchi, S.; Terada, H.; Shinohara, Y.
Substitutions of three amino acids in human heart/muscle type carnitine palmitoyltransferase I caused by single nucleotide polymorphisms
Biochem. Genet.
46
54-63
2008
Homo sapiens
Manually annotated by BRENDA team
Matsuo, T.; Yamamoto, A.; Yamamoto, T.; Otsuki, K.; Yamazaki, N.; Kataoka, M.; Terada, H.; Shinohara, Y.
Replacement of C305 in Heart/Muscle-Type Isozyme of Human Carnitine Palmitoyltransferase I with Aspartic Acid and Other Amino Acids
Biochem. Genet.
48
193-201
2010
Homo sapiens
Manually annotated by BRENDA team
Bruce, C.R.; Hoy, A.J.; Turner, N.; Watt, M.J.; Allen, T.L.; Carpenter, K.; Cooney, G.J.; Febbraio, M.A.; Kraegen, E.W.
Overexpression of carnitine palmitoyltransferase-1 in skeletal muscle is sufficient to enhance fatty acid oxidation and improve high-fat diet-induced insulin resistance
Diabetes
58
550-558
2009
Homo sapiens (Q92523)
Manually annotated by BRENDA team
Relat, J.; Pujol-Vidal, M.; Haro, D.; Marrero, P.F.
A characteristic Glu17 residue of pig carnitine palmitoyltransferase 1 is responsible for the low Km for carnitine and the low sensitivity to malonyl-CoA inhibition of the enzyme
FEBS J.
276
210-218
2009
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Yao, D.; Mizuguchi, H.; Yamaguchi, M.; Yamada, H.; Chida, J.; Shikata, K.; Kido, H.
Thermal instability of compound variants of carnitine palmitoyltransferase II and impaired mitochondrial fuel utilization in influenza-associated encephalopathy
Hum. Mutat.
29
718-727
2008
Homo sapiens (P23786), Homo sapiens
Manually annotated by BRENDA team
Roomets, E.; Kivelae, T.; Tyni, T.
Carnitine palmitoyltransferase I and Acyl-CoA dehydrogenase 9 in retina: insights of retinopathy in mitochondrial trifunctional protein defects
Invest. Ophthalmol. Vis. Sci.
49
1660-1664
2008
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Greenberg, C.R.; Dilling, L.A.; Thompson, G.R.; Seargeant, L.E.; Haworth, J.C.; Phillips, S.; Chan, A.; Vallance, H.D.; Waters, P.J.; Sinclair, G.; Lillquist, Y.; Wanders, R.J.; Olpin, S.E.
The paradox of the carnitine palmitoyltransferase type Ia P479L variant in Canadian Aboriginal populations
Mol. Genet. Metab.
96
201-207
2009
Homo sapiens
Manually annotated by BRENDA team
Violante, S.; Ijlst, L.; van Lenthe, H.; de Almeida, I.T.; Wanders, R.J.; Ventura, F.V.
Carnitine palmitoyltransferase 2: New insights on the substrate specificity and implications for acylcarnitine profiling
Biochim. Biophys. Acta
1802
728-732
2010
Homo sapiens (P23786), Homo sapiens
Manually annotated by BRENDA team
Zaugg, K.; Yao, Y.; Reilly, P.T.; Kannan, K.; Kiarash, R.; Mason, J.; Huang, P.; Sawyer, S.K.; Fuerth, B.; Faubert, B.; Kalliomaeki, T.; Elia, A.; Luo, X.; Nadeem, V.; Bungard, D.; Yalavarthi, S.; Growney, J.D.; Wakeham, A.; Moolani, Y.; Silvester, J.; Ten, A.Y.; Bakker, W.; Tsuchihara, K.; Berger, S.L.; H, H.i.
Carnitine palmitoyltransferase 1C promotes cell survival and tumor growth under conditions of metabolic stress
Genes Dev.
25
1041-1051
2011
Mus musculus (Q8BGD5), Mus musculus, Homo sapiens (Q8TCG5), Homo sapiens
Manually annotated by BRENDA team
Violante, S.; Ijlst, L.; Ruiter, J.; Koster, J.; van Lenthe, H.; Duran, M.; de Almeida, I.T.; Wanders, R.J.; Houten, S.M.; Ventura, F.V.
Substrate specificity of human carnitine acetyltransferase: Implications for fatty acid and branched-chain amino acid metabolism
Biochim. Biophys. Acta
1832
773-779
2013
Homo sapiens (P23786), Homo sapiens
Manually annotated by BRENDA team
Violante, S.; Ijlst, L.; Te Brinke, H.; Tavares de Almeida, I.; Wanders, R.J.; Ventura, F.V.; Houten, S.M.
Carnitine palmitoyltransferase 2 and carnitine/acylcarnitine translocase are involved in the mitochondrial synthesis and export of acylcarnitines
FASEB J.
27
2039-2044
2013
Homo sapiens (P23786), Homo sapiens
Manually annotated by BRENDA team
Setoyama, D.; Fujimura, Y.; Miura, D.
Metabolomics reveals that carnitine palmitoyltransferase-1 is a novel target for oxidative inactivation in human cells
Genes Cells
18
1107-1119
2013
Homo sapiens
Manually annotated by BRENDA team
Pucci, S.; Zonetti, M.J.; Fisco, T.; Polidoro, C.; Bocchinfuso, G.; Palleschi, A.; Novelli, G.; Spagnoli, L.G.; Mazzarelli, P.
Carnitine palmitoyl transferase-1A (CPT1A): a new tumor specific target in human breast cancer
Oncotarget
12
19982-19996
2016
Homo sapiens (P50416), Homo sapiens
Manually annotated by BRENDA team
Yao, M.; Cai, M.; Yao, D.; Xu, X.; Yang, R.; Li, Y.; Zhang, Y.; Kido, H.; Yao, D.
Abbreviated half-lives and impaired fuel utilization in carnitine palmitoyltransferase II variant fibroblasts
PLoS ONE
10
e0119936
2015
Homo sapiens (P23786), Homo sapiens
Manually annotated by BRENDA team
Menezes dos Reis, L.; Adamoski, D.; Ornitz Oliveira Souza, R.; Rodrigues Ascencao, C.F.; Sousa de Oliveira, K.R.; Correa-da-Silva, F.; Malta de Sa Patroni, F.; Meira Dias, M.; Consonni, S.R.; Mendes de Moraes-Vieira, P.M.; Silber, A.M.; Dias, S.M.G.
Dual inhibition of glutaminase and carnitine palmitoyltransferase decreases growth and migration of glutaminase inhibition-resistant triple-negative breast cancer cells
J. Biol. Chem.
294
9342-9357
2019
Homo sapiens, Homo sapiens (P23786)
Manually annotated by BRENDA team
Guan, L.; Chen, Y.; Wang, Y.; Zhang, H.; Fan, S.; Gao, Y.; Jiao, T.; Fu, K.; Sun, J.; Yu, A.; Huang, M.; Bi, H.
Effects of carnitine palmitoyltransferases on cancer cellular senescence
J. Cell. Physiol.
234
1707-1719
2019
Homo sapiens (P23786), Homo sapiens (Q8TCG5), Homo sapiens (Q92523)
Manually annotated by BRENDA team
Motlagh, L.; Golbik, R.; Sippl, W.; Zierz, S.
Stabilization of the thermolabile variant S113L of carnitine palmitoyltransferase II
Neurol. Genet.
2
e53
2016
Homo sapiens (P23786)
Manually annotated by BRENDA team
Lee, J.; Hyon, J.; Min, J.; Huh, Y.; Kim, H.; Lee, H.; Yun, S.; Choi, C.; Jeong Ha, S.; Park, J.; Chung, Y.; Jeong, H.; Ha, S.; Jung, S.; Kim, Y.; Han, E.
Mitochondrial carnitine palmitoyltransferase 2 is involved in Nepsilon-(carboxymethyl)-lysine-mediated diabetic nephropathy
Pharmacol. Res.
152
104600
2020
Homo sapiens (P23786), Homo sapiens
Manually annotated by BRENDA team
Yao, C.H.; Liu, G.Y.; Wang, R.; Moon, S.H.; Gross, R.W.; Patti, G.J.
Identifying off-target effects of etomoxir reveals that carnitine palmitoyltransferase I is essential for cancer cell proliferation independent of beta-oxidation
PLoS Biol.
16
e2003782
2018
Homo sapiens (P50416)
Manually annotated by BRENDA team
Calderon-Dominguez, M.; Sebastian, D.; Fucho, R.; Weber, M.; Mir, J.F.; Garcia-Casarrubios, E.; Obregon, M.J.; Zorzano, A.; Valverde, A.M.; Serra, D.; Herrero, L.
Carnitine palmitoyltransferase 1 increases lipolysis, UCP1 protein expression and mitochondrial activity in brown adipocytes
PLoS ONE
11
e0159399
2016
Homo sapiens (P50416), Homo sapiens
Manually annotated by BRENDA team